In this work, the molecular dynamics (MD) method was used for the study of the interaction of bovine carbonic anhydrase with sodium dodecyl sulfate (SDS), with emphasis on the role of the charges of lysine side chains. For this purpose, bovine carbonic anhydrase was considered in two forms, namely BCA (with eighteen lysine-NH2 groups) and BCA-H (with eighteen lysine- + 3 NH groups). Simulation of each of these proteins was performed in two different concentrations of SDS. The following parameters: root mean square deviation of C-alpha of backbone, radius of gyration, hydrophobic solvent accessible surface area and the number of protein hydrogen bonds were calculated for BCA and BCA-H in the two concentrations of SDS. With regard to these parameters, no considerable differences were observed between BCA and BCA-H. In spite of the noted similar behavior, it was specified that these two structures were different concernin

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